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The Journal of Immunology, 1998, 161: 1371-1379.
Copyright © 1998 by The American Association of Immunologists

Cytokine-Like Factor-1, a Novel Soluble Protein, Shares Homology with Members of the Cytokine Type I Receptor Family1

Greg C. A. Elson2, Pierre Graber3, Christophe Losberger3, Suzanne Herren3, Denise Gretener3, Laurent N. Menoud3, Timothy N. C. Wells3, Marie H. Kosco-Vilbois3,4 and Jean-François Gauchat2

Department of Immunology, Geneva Biomedical Research Institute, Glaxo Wellcome Research and Development, Plan-les-Ouates, Switzerland

In this report we describe the identification, cloning, and expression pattern of human cytokine-like factor 1 (hCLF-1) and the identification and cloning of its murine homologue. They were identified from expressed sequence tags using amino acid sequences from conserved regions of the cytokine type I receptor family. Human CLF-1 and murine CLF-1 shared 96% amino acid identity and significant homology with many cytokine type I receptors. CLF-1 is a secreted protein, suggesting that it is either a soluble subunit within a cytokine receptor complex, like the soluble form of the IL-6R {alpha}-chain, or a subunit of a multimeric cytokine, e.g., IL-12 p40. The highest levels of hCLF-1 mRNA were observed in lymph node, spleen, thymus, appendix, placenta, stomach, bone marrow, and fetal lung, with constitutive expression of CLF-1 mRNA detected in a human kidney fibroblastic cell line. In fibroblast primary cell cultures, CLF-1 mRNA was up-regulated by TNF-{alpha}, IL-6, and IFN-{gamma}. Western blot analysis of recombinant forms of hCLF-1 showed that the protein has the tendency to form covalently linked di- and tetramers. These results suggest that CLF-1 is a novel soluble cytokine receptor subunit or part of a novel cytokine complex, possibly playing a regulatory role in the immune system and during fetal development.




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